Search results for "Bacterial adhesin"

showing 10 items of 21 documents

Molecular basis of endothelial dysfunction in sepsis.

2003

Sepsis is one of the major causes of mortality in critically ill patients and develops as a result of the host response to infection. A complex network of events is set into motion in the body by the infection and results in the pathogenesis of sepsis. This review article focuses on the molecular mechanisms and components involved in the pathogenesis of sepsis with a major emphasis on the endothelium. This includes sepsis-inducing bacterial components (e.g. endotoxins), cellular targets of these molecules and their responses, host reactions, intracellular and cytokine networks, individual susceptibility and new therapeutic targets in sepsis treatment.

MaleEndotheliumPhysiologymedicine.medical_treatmentReceptors Cell SurfaceBiologyNitric OxidePathogenesisSepsisPhysiology (medical)SepsismedicineHumansEndothelial dysfunctionHypoxiaMembrane GlycoproteinsToll-Like ReceptorsEndothelial Cellsmedicine.diseaseReview articleBacterial adhesinEndotoxinsmedicine.anatomical_structureCytokineImmunologyMutationCytokinesFemaleDisease SusceptibilityEndothelium VascularCardiology and Cardiovascular MedicineReactive Oxygen SpeciesCell Adhesion MoleculesIntracellularInterleukin-1Cardiovascular research
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Serologic Response to Cell Wall Mannoproteins and Proteins of Candida albicans

1998

SUMMARY The cell wall of Candida albicans not only is the structure in which many biological functions essential for the fungal cells reside but also is a significant source of candidal antigens. The major cell wall components that elicit a response from the host immune system are proteins and glycoproteins, the latter being predominantly mannoproteins. Both the carbohydrate and protein moieties are able to trigger immune responses. Although cell-mediated immunity is often considered to be the most important line of defense against candidiasis, cell wall protein and glycoprotein components also elicit a potent humoral response from the host that may include some protective antibodies. Prot…

Microbiology (medical)Antigens FungalEpidemiologyBiologyArticleMicrobiologyFungal ProteinsImmune systemAntigenCell WallCandida albicansAnimalsHumansCandida albicanschemistry.chemical_classificationFungal proteinMembrane GlycoproteinsGeneral Immunology and MicrobiologyPublic Health Environmental and Occupational Healthbiology.organism_classificationBacterial adhesinInfectious DiseaseschemistryHumoral immunityImmunologybiology.proteinAntibodyGlycoproteinClinical Microbiology Reviews
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Antibody response toCandida albicanscell wall antigens

2003

The cell wall of Candida albicans is not only the structure where many essential biological functions reside but is also a significant source of candidal antigens. The major cell wall components that elicit a response from the host immune system are proteins and glycoproteins, the latter being predominantly mannoproteins. Both carbohydrate and protein moieties are able to trigger immune responses. Proteins and glycoproteins exposed at the most external layers of the wall structure are involved in several types of interactions of fungal cells with the exocellular environment. Thus, coating of fungal cells with host antibodies has the potential to profoundly influence the host-parasite intera…

Microbiology (medical)Antigens FungalImmunologyMicrobiologyMicrobiologyImmune systemAntigenCell WallCandida albicansHumansImmunology and AllergyCandida albicansAntibodies Fungalchemistry.chemical_classificationbiologyCandidiasisGeneral Medicinebiology.organism_classificationDisseminated CandidiasisCorpus albicansBacterial adhesinInfectious DiseaseschemistryImmunologybiology.proteinAntibodyGlycoproteinFEMS Immunology & Medical Microbiology
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Anti-adhesion agents against Gram-positive pathogens

2014

The rise of antibiotic-resistance as well as the deficiency of investments by pharmaceutical companies in the development of new antibiotics, have stimulated the investigation of alternative strategies to conventional antibiotics for counteracting the pathogens. A fundamental step of Gram positive pathogenesis is the bacterial adhesion to the host tissue involving a direct and a specific interaction between bacterial surface molecules and host ligands. Targeting the adhesion is a good strategy to design novel anti-infective drugs agents useful to interfere with the pathogenic process and with a virulence mechanism as biofilm formation. This review is focused on anti-virulence compounds whic…

Microbiology (medical)Antivirulencemedicine.drug_classAntibioticsAdhesionBiologyGram-Positive BacteriaAntimicrobialHost tissueSettore BIO/19 - Microbiologia GeneraleMicrobiologyBacterial AdhesionAnti-Bacterial AgentsMicrobiologyBacterial proteinBacterial adhesinSortase ADrug DiscoverymedicineAnti-adhesion agents antivirulence drugs Gram-positive pathogens
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Characteristics of Escherichia coli strains belonging to enteropathogenic E. coli serogroups isolated in Italy from children with diarrhea.

1996

Fifty-five Escherichia coli strains belonging to enteropathogenic E. coli (EPEC) serogroups were examined for phenotypic and genetic factors associated with virulence. The strains were isolated in Italy from children with diarrhea and identified as EPEC by clinical laboratories using commercially available antisera. O:H serotyping showed that 35 strains (27 of O26, O111, and O128 serogroups) belonged to 11 serotypes considered to be classical EPEC O:H serotypes. The other 20 isolates were classified as 15 nonclassical EPEC O:H serotypes. All the potential EPEC virulence factors associated with bacterial adhesion (localized adherence, fluorescentactin staining test positivity, presence of th…

Microbiology (medical)SerotypeDiarrheaVirulencemedicine.disease_causeMicrobiologyPlasmidGenotypemedicineEscherichia coliHumansSerotypingAdhesins BacterialChildEscherichia colibiologyVirulenceHybridization probeEscherichia coli Proteinsbiology.organism_classificationbacterial infections and mycosesEnterobacteriaceaeVirologyBacterial adhesinbacteriaCarrier ProteinsBacterial Outer Membrane ProteinsPlasmidsResearch ArticleJournal of clinical microbiology
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BB0172, a Borrelia burgdorferi Outer Membrane Protein That Binds Integrin Α3Β1

2013

ABSTRACT Lyme disease is a multisystemic disorder caused by Borrelia burgdorferi infection. Upon infection, some B. burgdorferi genes are upregulated, including members of the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) protein family, which facilitate B. burgdorferi adherence to extracellular matrix components of the host. Comparative genome analysis has revealed a new family of B. burgdorferi proteins containing the von Willebrand factor A (vWFA) domain. In the present study, we characterized the expression and membrane association of the vWFA domain-containing protein BB0172 by using in vitro transcription/translation systems in the presence of microsomal …

Models MolecularProtein familyMolecular Sequence DataIntegrinBiologyModels BiologicalMicrobiologyBiotecnologiaMicrobiologyAmino Acid SequenceBorrelia burgdorferiAdhesins BacterialMolecular BiologyIntegrin alpha3beta1Borrelia Burgdorferi InfectionProteïnes de membranaIntegrin alpha3beta1Articlesbiology.organism_classificationCell biologyBacterial adhesinBorrelia burgdorferibiology.proteinMSCRAMMBacterial outer membraneSequence AlignmentBacterial Outer Membrane ProteinsProtein Binding
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Rapid and specific detection of F17-related pilin and adhesin genes in diarrheic and septicemic Escherichia coli strains by multiplex PCR

1996

The F17-related adhesins are prevalent in Escherichia coli strains isolated from calves with diarrhea or septicemia and from lambs with nephropathy. The F17 family includes the F17a, F17b, F17c, and F111 fimbriae produced by bovine E. coli strains and the G agglutinin produced by human uropathogenic E. coli strains. An easy and inexpensive multiplex PCR method was developed to detect all the F17-related fimbriae and to identify four subtypes of structural subunit genes and two distinct subfamilies of adhesin genes by only two runs of amplification. A strict correlation was observed between the phenotypic assays and the multiplex PCR method when 166 pathogenic E. coli strains isolated from i…

OperonFimbriaBacteremiamedicine.disease_causePolymerase Chain ReactionPilusFimbriae ProteinsEscherichia coli InfectionsComputingMilieux_MISCELLANEOUS2. Zero hunger0303 health sciencesbiologyEnterobacteriaceae3. Good healthPhenotype[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyMultigene FamilyFimbriae ProteinsBacterial Outer Membrane ProteinsResearch ArticleDiarrheaMicrobiology (medical)Gene Transfer HorizontalCattle DiseasesSheep DiseasesMicrobiology03 medical and health sciencesSpecies SpecificityOperonEscherichia colimedicineAnimalsHumansAdhesins BacterialEscherichia coli[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyDNA Primers030304 developmental biologyBacteriological TechniquesSheepBase Sequence030306 microbiologyTOXINE CNF2biochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyFIMBRIAE F17Bacterial adhesinGenes BacterialPilinbiology.proteinbacteriaCattle
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AF/R2 adhesin and cytopathic effect as virulence traits of diarrhea-inducing Escherichia coli O103 in European rabbit

1995

Escherichia coli strains belonging to 0103:K-:H2 serovar and rhamnose negative biovars are responsible for frequent life-threatening diarrheas in weaned rabbits from national breeding units in western Europe (Blanco et al., 1994; Camguilhem and A. Milon, 1989). According to their mechanisms of pathogenesis, these strains may be considered as enteropathogenic E. coli (EPEC)-like. They adhere to intestinal brush border and to HeLa cells by mean of an adhesin called AF/R2 (Adhesive Factor/Rabbit 2) (Milon et al., 1990). They do not produce known toxins (i.e. ST, LT, SLT, CNF, CLDT) (Blanco et al., 1994; Mariani-Kurkdjian et al., 1993) and bear sequences homologous to EPEC eaeA (Leroy et al., 1…

Serotype0303 health sciencesBrush border030306 microbiologyRhamnose[SDV]Life Sciences [q-bio]VirulenceBiologymedicine.disease_cause3. Good healthMicrobiologyBacterial adhesin[SDV] Life Sciences [q-bio]03 medical and health scienceschemistry.chemical_compoundchemistryGiant cellmedicineEscherichia coliComputingMilieux_MISCELLANEOUS030304 developmental biologyCytopathic effect
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F17-like fimbriae from an invasive Escherichia coli strain producing cytotoxic necrotizing factor type 2 toxin

1994

The F17b fimbriae encoded by the transmissible virulence plasmid Vir, also coding for cytotoxic necrotizing factor type 2, were characterized. A 5.7-kb region of Vir mediates in vitro N-acetylglucosamine-sensitive adhesion to calf intestinal villi. Sequence analysis revealed that this region codes for a structural subunit and an adhesin closely related to the F17-A and F17-G proteins encoded by the F17 fimbrial gene cluster. The F17b-A gene presents an open reading frame of 540 bp encoding a polypeptide of 180 amino acids with a putative signal peptide of 21 residues. The mature protein shows an identity of 74% with the F17-A structural subunit. This 20-kDa protein is recognized by antiseru…

Signal peptideVirulence Factors[SDV]Life Sciences [q-bio]Bacterial ToxinsMolecular Sequence DataImmunologyFimbriaMutantBiologymedicine.disease_causeMicrobiologyMicrobiologyBacterial ProteinsGene clusterEscherichia colimedicineAmino Acid SequenceEscherichia coliPeptide sequenceAdhesins Escherichia coliAntigens BacterialBase SequenceCytotoxinsEscherichia coli ProteinsSEQUENCE NULECOTIDIQUEbiochemical phenomena metabolism and nutritionMolecular biology[SDV] Life Sciences [q-bio]Bacterial adhesinOpen reading frameInfectious DiseasesFimbriae BacterialCLONAGE DE GENEParasitologyResearch ArticleBacterial Outer Membrane ProteinsPlasmidsInfection and Immunity
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The hemagglutinin of Staphylococcus saprophyticus is a major adhesin for uroepithelial cells.

1996

The 160-kDa hemagglutinin of Staphylococcus saprophyticus also serves as a fibronectin-binding protein, and the two activities may be present on different parts of the molecule. Bacteria expressing the 160-kDa hemagglutinin bound in large numbers to histological sections of human ureters, whereas nonhemagglutinating bacteria did not bind. Binding was decreased by an antiserum to the 160-kDa protein and by a preparation of sheep erythrocyte membranes. Fibronectin had no effect. We therefore conclude that binding of S. saprophyticus to uroepithelial cells is mediated by the hemagglutinating activity of the 160-kDa surface protein.

StaphylococcusImmunologyBiologymedicine.disease_causeMicrobiologyBacterial AdhesionEpitheliumMicrobiologymedicineAnimalsHumansAntiserumchemistry.chemical_classificationStaphylococcus saprophyticusSheepBinding proteinErythrocyte MembraneHemagglutininbiology.organism_classificationFibronectinsBacterial adhesinInfectious DiseasesHemagglutininschemistryParasitologyUreterGlycoproteinStaphylococcusBacteriaResearch ArticleInfection and immunity
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